CAC1A_RAT
ID CAC1A_RAT Reviewed; 2212 AA.
AC P54282; Q01541;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Voltage-dependent P/Q-type calcium channel subunit alpha-1A;
DE AltName: Full=Brain calcium channel I;
DE Short=BI;
DE AltName: Full=Calcium channel, L type, alpha-1 polypeptide, isoform 4;
DE AltName: Full=Rat brain class A;
DE Short=RBA-I;
DE AltName: Full=Voltage-gated calcium channel subunit alpha Cav2.1;
GN Name=Cacna1a; Synonyms=Cach4, Cacn3, Cacnl1a4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=1648226; DOI=10.1073/pnas.88.13.5621;
RA Starr T.V.B., Prystay W., Snutch T.P.;
RT "Primary structure of a calcium channel that is highly expressed in the rat
RT cerebellum.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:5621-5625(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1354-1659 (ISOFORM 2).
RC TISSUE=Kidney;
RX PubMed=1279681; DOI=10.1073/pnas.89.21.10494;
RA Yu A.S.L., Hebert S.C., Brenner B.M., Lytton J.;
RT "Molecular characterization and nephron distribution of a family of
RT transcripts encoding the pore-forming subunit of Ca2+ channels in the
RT kidney.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:10494-10498(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1435-1667 (ISOFORM 3).
RX PubMed=1692134; DOI=10.1073/pnas.87.9.3391;
RA Snutch T.P., Leonard J.P., Gilbert M.M., Lester H.A., Davidson N.;
RT "Rat brain expresses a heterogeneous family of calcium channels.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:3391-3395(1990).
RN [4]
RP FUNCTION, INTERACTION WITH SPIDER OMEGA-AGATOXIN-IVA, AND SUBUNIT.
RC TISSUE=Venom;
RX PubMed=1311418; DOI=10.1038/355827a0;
RA Mintz I.M., Venema V.J., Swiderek K.M., Lee T.D., Bean B.P., Adams M.E.;
RT "P-type calcium channels blocked by the spider toxin omega-Aga-IVA.";
RL Nature 355:827-829(1992).
RN [5]
RP INTERACTION WITH CABP1.
RX PubMed=11865310; DOI=10.1038/nn805;
RA Lee A., Westenbroek R.E., Haeseleer F., Palczewski K., Scheuer T.,
RA Catterall W.A.;
RT "Differential modulation of Ca(v)2.1 channels by calmodulin and Ca2+-
RT binding protein 1.";
RL Nat. Neurosci. 5:210-217(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453; SER-752; SER-755;
RP SER-1998; SER-2028; SER-2030; SER-2071 AND SER-2091, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry
CC of calcium ions into excitable cells and are also involved in a variety
CC of calcium-dependent processes, including muscle contraction, hormone
CC or neurotransmitter release, gene expression, cell motility, cell
CC division and cell death. The isoform alpha-1A gives rise to P and/or Q-
CC type calcium currents. P/Q-type calcium channels belong to the 'high-
CC voltage activated' (HVA) group and are specifically blocked by the
CC spider omega-agatoxin-IVA (AC P30288) (PubMed:1311418). They are
CC however insensitive to dihydropyridines (DHP).
CC {ECO:0000250|UniProtKB:O00555}.
CC -!- SUBUNIT: Voltage-dependent calcium channels are multisubunit complexes,
CC consisting of alpha-1, alpha-2, beta and delta subunits in a 1:1:1:1
CC ratio. The channel activity is directed by the pore-forming and
CC voltage-sensitive alpha-1 subunit. In many cases, this subunit is
CC sufficient to generate voltage-sensitive calcium channel activity. The
CC auxiliary subunits beta and alpha-2/delta linked by a disulfide bridge
CC regulate the channel activity (By similarity). Interacts (via C-
CC terminal CDB motif) with CABP1 in the pre- and postsynaptic membranes
CC (PubMed:11865310). Interacts with the spider omega-agatoxin-IVA (AC
CC P30288) (PubMed:1311418). {ECO:0000250|UniProtKB:O00555,
CC ECO:0000269|PubMed:11865310, ECO:0000269|PubMed:1311418}.
CC -!- INTERACTION:
CC P54282; P11275: Camk2a; NbExp=3; IntAct=EBI-3507416, EBI-2640645;
CC P54282; Q9JIR4: Rims1; NbExp=4; IntAct=EBI-3507416, EBI-3507436;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O00555};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=P54282-1; Sequence=Displayed;
CC Name=2; Synonyms=RKC8;
CC IsoId=P54282-2; Sequence=VSP_000881;
CC Name=3; Synonyms=RBA-65;
CC IsoId=P54282-3; Sequence=Not described;
CC Name=4;
CC IsoId=P54282-4; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: Brain specific. Purkinje cells contain
CC predominantly P-type VSCC, the Q-type being a prominent calcium current
CC in cerebellar granule cells. Also found in heart, in kidney distal
CC convoluted tubule (DCT), and in pituitary.
CC -!- DOMAIN: Each of the four internal repeats contains five hydrophobic
CC transmembrane segments (S1, S2, S3, S5, S6) and one positively charged
CC transmembrane segment (S4). S4 segments probably represent the voltage-
CC sensor and are characterized by a series of positively charged amino
CC acids at every third position.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. CACNA1A subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M64373; AAA40806.1; -; mRNA.
DR EMBL; M99222; AAA40896.1; -; mRNA.
DR PIR; A41098; A41098.
DR RefSeq; NP_037050.2; NM_012918.3.
DR AlphaFoldDB; P54282; -.
DR BMRB; P54282; -.
DR SMR; P54282; -.
DR BioGRID; 247433; 4.
DR CORUM; P54282; -.
DR DIP; DIP-29638N; -.
DR IntAct; P54282; 3.
DR STRING; 10116.ENSRNOP00000059641; -.
DR DrugCentral; P54282; -.
DR GuidetoPHARMACOLOGY; 532; -.
DR TCDB; 1.A.1.11.8; the voltage-gated ion channel (vic) superfamily.
DR GlyGen; P54282; 2 sites.
DR iPTMnet; P54282; -.
DR PhosphoSitePlus; P54282; -.
DR PaxDb; P54282; -.
DR PRIDE; P54282; -.
DR GeneID; 25398; -.
DR KEGG; rno:25398; -.
DR CTD; 773; -.
DR RGD; 2244; Cacna1a.
DR eggNOG; KOG2301; Eukaryota.
DR InParanoid; P54282; -.
DR OrthoDB; 172471at2759; -.
DR PhylomeDB; P54282; -.
DR Reactome; R-RNO-112308; Presynaptic depolarization and calcium channel opening.
DR Reactome; R-RNO-422356; Regulation of insulin secretion.
DR PRO; PR:P54282; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0042995; C:cell projection; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; IDA:SynGO.
DR GO; GO:0043025; C:neuronal cell body; IDA:ARUK-UCL.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:RGD.
DR GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
DR GO; GO:0008331; F:high voltage-gated calcium channel activity; IDA:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019905; F:syntaxin binding; ISO:RGD.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:UniProtKB.
DR GO; GO:0099626; F:voltage-gated calcium channel activity involved in regulation of presynaptic cytosolic calcium levels; ISO:RGD.
DR GO; GO:0007628; P:adult walking behavior; ISO:RGD.
DR GO; GO:0048266; P:behavioral response to pain; ISO:RGD.
DR GO; GO:0070509; P:calcium ion import; IDA:RGD.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0070588; P:calcium ion transmembrane transport; ISO:RGD.
DR GO; GO:0006816; P:calcium ion transport; IDA:RGD.
DR GO; GO:0048791; P:calcium ion-regulated exocytosis of neurotransmitter; ISO:RGD.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; ISO:RGD.
DR GO; GO:0008219; P:cell death; ISO:RGD.
DR GO; GO:0030644; P:cellular chloride ion homeostasis; ISO:RGD.
DR GO; GO:1904646; P:cellular response to amyloid-beta; ISO:RGD.
DR GO; GO:0021953; P:central nervous system neuron differentiation; ISO:RGD.
DR GO; GO:0021679; P:cerebellar molecular layer development; ISO:RGD.
DR GO; GO:0021702; P:cerebellar Purkinje cell differentiation; ISO:RGD.
DR GO; GO:0021680; P:cerebellar Purkinje cell layer development; ISO:RGD.
DR GO; GO:0021590; P:cerebellum maturation; ISO:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:RGD.
DR GO; GO:0048813; P:dendrite morphogenesis; ISO:RGD.
DR GO; GO:0014051; P:gamma-aminobutyric acid secretion; ISO:RGD.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; ISO:RGD.
DR GO; GO:0042593; P:glucose homeostasis; ISO:RGD.
DR GO; GO:0051899; P:membrane depolarization; ISO:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:0050883; P:musculoskeletal movement, spinal reflex action; ISO:RGD.
DR GO; GO:0032353; P:negative regulation of hormone biosynthetic process; ISO:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:0050877; P:nervous system process; ISO:RGD.
DR GO; GO:0050905; P:neuromuscular process; ISO:RGD.
DR GO; GO:0050885; P:neuromuscular process controlling balance; ISO:RGD.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; ISO:RGD.
DR GO; GO:0007270; P:neuron-neuron synaptic transmission; ISO:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR GO; GO:0043113; P:receptor clustering; ISO:RGD.
DR GO; GO:0014056; P:regulation of acetylcholine secretion, neurotransmission; ISO:RGD.
DR GO; GO:0050770; P:regulation of axonogenesis; ISO:RGD.
DR GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; ISO:RGD.
DR GO; GO:0010817; P:regulation of hormone levels; ISO:RGD.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR GO; GO:0001505; P:regulation of neurotransmitter levels; ISO:RGD.
DR GO; GO:0031335; P:regulation of sulfur amino acid metabolic process; ISO:RGD.
DR GO; GO:1901385; P:regulation of voltage-gated calcium channel activity; IMP:RGD.
DR GO; GO:1904645; P:response to amyloid-beta; ISO:RGD.
DR GO; GO:0048265; P:response to pain; ISO:RGD.
DR GO; GO:0060024; P:rhythmic synaptic transmission; ISO:RGD.
DR GO; GO:0019233; P:sensory perception of pain; IMP:RGD.
DR GO; GO:0021522; P:spinal cord motor neuron differentiation; ISO:RGD.
DR GO; GO:0007416; P:synapse assembly; ISO:RGD.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; ISO:RGD.
DR GO; GO:0019226; P:transmission of nerve impulse; ISO:RGD.
DR GO; GO:0021750; P:vestibular nucleus development; ISO:RGD.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR005448; CACNA1A.
DR InterPro; IPR031649; GPHH_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR014873; VDCC_a1su_IQ.
DR InterPro; IPR002077; VDCCAlpha1.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR Pfam; PF08763; Ca_chan_IQ; 1.
DR Pfam; PF16905; GPHH; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR PRINTS; PR00167; CACHANNEL.
DR PRINTS; PR01632; PQVDCCALPHA1.
DR SMART; SM01062; Ca_chan_IQ; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Calcium channel; Calcium transport;
KW Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..2212
FT /note="Voltage-dependent P/Q-type calcium channel subunit
FT alpha-1A"
FT /id="PRO_0000053919"
FT TOPO_DOM 1..100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..119
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..138
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..156
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..168
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..184
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..192
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..211
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..230
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..250
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..337
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..362
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 363..489
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 490..509
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 510..523
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 524..543
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 544..551
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 552..570
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 571..580
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 581..599
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 600..618
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 619..638
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 639..691
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 692..716
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 717..1190
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1191..1214
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1215..1231
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1232..1251
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1252..1258
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1259..1282
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1283..1293
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1294..1311
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1312..1330
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1331..1350
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1351..1437
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1438..1462
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1463..1518
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1519..1537
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1538..1551
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1552..1573
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1574..1580
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1581..1600
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1601..1607
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1608..1626
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1627..1645
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1646..1665
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1666..1737
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1738..1763
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1764..2212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 87..365
FT /note="I"
FT REPEAT 475..719
FT /note="II"
FT REPEAT 1182..1465
FT /note="III"
FT REPEAT 1502..1765
FT /note="IV"
FT REGION 385..402
FT /note="Binding to the beta subunit"
FT /evidence="ECO:0000250"
FT REGION 814..1117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1137..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1940..2212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..864
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..991
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1011
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1081
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1947..1962
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1974..1995
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2007..2021
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2059..2075
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2086..2105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2156..2173
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2174..2212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 320
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT BINDING 670
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT BINDING 1411
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P07293"
FT SITE 1600
FT /note="Binds to omega-Aga-IVA"
FT /evidence="ECO:0000250"
FT MOD_RES 411
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P97445"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97445"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 752
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 755
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 792
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97445"
FT MOD_RES 1038
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97445"
FT MOD_RES 1042
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97445"
FT MOD_RES 1051
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97445"
FT MOD_RES 1935
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P97445"
FT MOD_RES 1998
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2016
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97445"
FT MOD_RES 2028
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2030
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2071
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2091
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1607
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1602
FT /note="G -> GNP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1279681"
FT /id="VSP_000881"
SQ SEQUENCE 2212 AA; 251527 MW; DFBD7A0F553AFA52 CRC64;
MARFGDEMPG RYGAGGGGSG PAAGVVVGAA GGRGAGGSRQ GGQPGAQRMY KQSMAQRART
MALYNPIPVR QNCLTVNRSL FLFSEDNVVR KYAKKITEWP PFEYMILATI IANCIVLALE
QHLPDDDKTP MSERLDDTEP YFIGIFCFEA GIKIVALGFA FHKGSYLRNG WNVMDFVVVL
TGILATVGTE FDLRTLRAVR VLRPLKLVSG IPSLQVVLKS IMKAMIPLLQ IGLLLFFAIL
IFAIIGLEFY MGKFHTTCFE EGTDDIQGES PAPCGTEEPA RTCPNGTKCQ PYWEGPNNGI
TQFDNILFAV LTVFQCITME GWTDLLYNSN DASGNTWNWL YFIPLIIIGS FFMLNLVLGV
LSGEFAKERE RVENRRAFLK LRRQQQIERE LNGYMEWISK AEEVILAEDE TDVEQRHPFD
GALRRATLKK SKTDLLNPEE AEDQLADIAS VGSPFARASI KSAKLENSTF FHKKERRMRF
YIRRMVKTQA FYWTVLSLVA LNTLWLAIVH YNQPEWLSDF LYYAEFIFLG LFMSEMFIKM
YGLGTRPYFH SSFNCFDCGV IIGSIFEVIW AVIKPGTSFG ISVLRALRLL RIFKVTKYWA
SLRNLVVSLL NSMKSIISLL FLLFLFIVVF ALLGMQLFGG QFNFDEGTPP TNFDTFPAAI
MTVFQILTGE DWNEVMYDEI KSQGGVQGGM VFSIYFIVLT LFGNYTLLNV FLAIAVDNLA
NAQELTKDEQ EEEEAANQKL ALQKAKEVAE VSPLSAANMS IAVKEQQKNQ KPAKSVWEQR
TSEMRKQNLL ASREALYGDA AERWPTTYAR PLRPDVKTHL DRPLVVDPQE NRNNNTNKSR
APEALRQTAR PRESARDPDA RRAWPSSPER APGREGPYGR ESEPQQREHA PPREHVPWDA
DPERAKAGDA PRRHTHRPVA EGEPRRHRAR RRPGDEPDDR PERRPRPRDA TRPARAADGE
GDDGERKRRH RHGPPAHDDR ERRHRRRKES QGSGVPMSGP NLSTTRPIQQ DLGRQDLPLA
EDLDNMKNNK LATGEPASPH DSLGHSGLPP SPAKIGNSTN PGPALATNPQ NAASRRTPNN
PGNPSNPGPP KTPENSLIVT NPSSTQPNSA KTARKPEHMA VEIPPACPPL NHTVVQVNKN
ANPDPLPKKE EEKKEEEEAD PGEDGPKPMP PYSSMFILST TNPLRRLCHY ILNLRYFEMC
ILMVIAMSSI ALAAEDPVQP NAPRNNVLRY FDYVFTGVFT FEMVIKMIDL GLVLHQGAYF
RDLWNILDFI VVSGALVAFA FTGNSKGKDI NTIKSLRVLR VLRPLKTIKR LPKLKAVFDC
VVNSLKNVFN ILIVYMLFMF IFAVVAVQLF KGKFFHCTDE SKEFERDCRG KYLLYEKNEV
KARDREWKKY DFHYDNVLWA LLTLFTVSTG EGWPQVLKHS VDATFENQGP SPGYRMEMSI
FYVVYFVVFP FFFVNIFVAL IIITFQEQGD KMMEEYSLEK NERACIDFAI SAKPLTRHMP
QNKQSFQYRM WQFVVSPPFE YTIMAMIALN TIVLMMKFYG ASVAYENALR VFNIVFTSLF
SLECVLKVMA FGILNYFRDA WNIFDFVTVL GSITDILVTE FGNNFINLSF LRLFRAARLI
KLLRQGYTIR ILLWTFVQSF KALPYVCLLI AMLFFIYAII GMQVFGNIGI DGEDEDSDED
EFQITEHNNF RTFFQALMLL FRSATGEAWH NIMLSCLSGK PCDKNSGIQK PECGNEFAYF
YFVSFIFLCS FLMLNLFVAV IMDNFEYLTR DSSILGPHHL DEYVRVWAEY DPAACGRIHY
KDMYSLLRVI SPPLGLGKKC PHRVACKRLL RMDLPVADDN TVHFNSTLMA LIRTALDIKI
AKGGADKQQM DAELRKEMMA IWPNLSQKTL DLLVTPHKST DLTVGKIYAA MMIMEYYRQS
KAKKLQAMRE EQNRTPLMFQ RMEPPSPTQE GGPSQNALPS TQLDPGGGLM AQESSMKESP
SWVTQRAQEM FQKTGTWSPE RGPPIDMPNS QPNSQSVEMR EMGTDGYSDS EHYLPMEGQT
RAASMPRLPA ENQRRRGRPR GNNLSTISDT SPMKRSASVL GPKARRLDDY SLERVPPEEN
QRYHQRRRDR GHRTSERSLG RYTDVDTGLG TDLSMTTQSG DLPSKDRDQD RGRPKDRKHR
PHHHHHHHHH HPPAPDRERY AQERPDTGRA RAREQRWSRS PSEGREHATH RQ
